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Anserine is expressed in human cardiac and skeletal muscles

We evaluated whether anserine, a methylated analog of the dipeptide carnosine, is present in the cardiac and skeletal muscles of humans and whether the CARNMT1 gene, which encodes the anserine synthesizing enzyme carnosine‐N‐methyltransferase, is expressed in human skeletal muscle. We found that ans...

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Detalles Bibliográficos
Autores principales: de Souza Gonçalves, Lívia, Pereira, Wagner Ribeiro, da Silva, Rafael Pires, Yamaguchi, Guilherme Carvalho, Carvalho, Victor Henrique, Vargas, Bianca Scigliano, Jensen, Leonardo, de Medeiros, Marisa Helena Gennari, Roschel, Hamilton, Artioli, Guilherme Giannini
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539627/
https://www.ncbi.nlm.nih.gov/pubmed/37771070
http://dx.doi.org/10.14814/phy2.15833
Descripción
Sumario:We evaluated whether anserine, a methylated analog of the dipeptide carnosine, is present in the cardiac and skeletal muscles of humans and whether the CARNMT1 gene, which encodes the anserine synthesizing enzyme carnosine‐N‐methyltransferase, is expressed in human skeletal muscle. We found that anserine is present at low concentrations (low micromolar range) in both cardiac and skeletal muscles, and that anserine content in skeletal muscle is ~15 times higher than in cardiac muscle (cardiac muscle: 10.1 ± 13.4 μmol·kg(−1) of dry muscle, n = 12; skeletal muscle: 158.1 ± 68.5 μmol·kg(−1) of dry muscle, n = 11, p < 0.0001). Anserine content in the heart was highly variable between individuals, ranging from 1.4 to 45.4 μmol·kg(−1) of dry muscle, but anserine content was not associated with sex, age, or body mass. We also showed that CARNMT1 gene is poorly expressed in skeletal muscle (n = 10). This is the first study to demonstrate that anserine is present in the ventricle of the human heart. The presence of anserine in human heart and the confirmation of its expression in human skeletal muscle open new avenues of investigation on the specific and differential physiological functions of histidine dipeptides in striated muscles.